-
Notifications
You must be signed in to change notification settings - Fork 2
/
1mlz.pdb
7895 lines (7895 loc) · 625 KB
/
1mlz.pdb
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36
37
38
39
40
41
42
43
44
45
46
47
48
49
50
51
52
53
54
55
56
57
58
59
60
61
62
63
64
65
66
67
68
69
70
71
72
73
74
75
76
77
78
79
80
81
82
83
84
85
86
87
88
89
90
91
92
93
94
95
96
97
98
99
100
101
102
103
104
105
106
107
108
109
110
111
112
113
114
115
116
117
118
119
120
121
122
123
124
125
126
127
128
129
130
131
132
133
134
135
136
137
138
139
140
141
142
143
144
145
146
147
148
149
150
151
152
153
154
155
156
157
158
159
160
161
162
163
164
165
166
167
168
169
170
171
172
173
174
175
176
177
178
179
180
181
182
183
184
185
186
187
188
189
190
191
192
193
194
195
196
197
198
199
200
201
202
203
204
205
206
207
208
209
210
211
212
213
214
215
216
217
218
219
220
221
222
223
224
225
226
227
228
229
230
231
232
233
234
235
236
237
238
239
240
241
242
243
244
245
246
247
248
249
250
251
252
253
254
255
256
257
258
259
260
261
262
263
264
265
266
267
268
269
270
271
272
273
274
275
276
277
278
279
280
281
282
283
284
285
286
287
288
289
290
291
292
293
294
295
296
297
298
299
300
301
302
303
304
305
306
307
308
309
310
311
312
313
314
315
316
317
318
319
320
321
322
323
324
325
326
327
328
329
330
331
332
333
334
335
336
337
338
339
340
341
342
343
344
345
346
347
348
349
350
351
352
353
354
355
356
357
358
359
360
361
362
363
364
365
366
367
368
369
370
371
372
373
374
375
376
377
378
379
380
381
382
383
384
385
386
387
388
389
390
391
392
393
394
395
396
397
398
399
400
401
402
403
404
405
406
407
408
409
410
411
412
413
414
415
416
417
418
419
420
421
422
423
424
425
426
427
428
429
430
431
432
433
434
435
436
437
438
439
440
441
442
443
444
445
446
447
448
449
450
451
452
453
454
455
456
457
458
459
460
461
462
463
464
465
466
467
468
469
470
471
472
473
474
475
476
477
478
479
480
481
482
483
484
485
486
487
488
489
490
491
492
493
494
495
496
497
498
499
500
501
502
503
504
505
506
507
508
509
510
511
512
513
514
515
516
517
518
519
520
521
522
523
524
525
526
527
528
529
530
531
532
533
534
535
536
537
538
539
540
541
542
543
544
545
546
547
548
549
550
551
552
553
554
555
556
557
558
559
560
561
562
563
564
565
566
567
568
569
570
571
572
573
574
575
576
577
578
579
580
581
582
583
584
585
586
587
588
589
590
591
592
593
594
595
596
597
598
599
600
601
602
603
604
605
606
607
608
609
610
611
612
613
614
615
616
617
618
619
620
621
622
623
624
625
626
627
628
629
630
631
632
633
634
635
636
637
638
639
640
641
642
643
644
645
646
647
648
649
650
651
652
653
654
655
656
657
658
659
660
661
662
663
664
665
666
667
668
669
670
671
672
673
674
675
676
677
678
679
680
681
682
683
684
685
686
687
688
689
690
691
692
693
694
695
696
697
698
699
700
701
702
703
704
705
706
707
708
709
710
711
712
713
714
715
716
717
718
719
720
721
722
723
724
725
726
727
728
729
730
731
732
733
734
735
736
737
738
739
740
741
742
743
744
745
746
747
748
749
750
751
752
753
754
755
756
757
758
759
760
761
762
763
764
765
766
767
768
769
770
771
772
773
774
775
776
777
778
779
780
781
782
783
784
785
786
787
788
789
790
791
792
793
794
795
796
797
798
799
800
801
802
803
804
805
806
807
808
809
810
811
812
813
814
815
816
817
818
819
820
821
822
823
824
825
826
827
828
829
830
831
832
833
834
835
836
837
838
839
840
841
842
843
844
845
846
847
848
849
850
851
852
853
854
855
856
857
858
859
860
861
862
863
864
865
866
867
868
869
870
871
872
873
874
875
876
877
878
879
880
881
882
883
884
885
886
887
888
889
890
891
892
893
894
895
896
897
898
899
900
901
902
903
904
905
906
907
908
909
910
911
912
913
914
915
916
917
918
919
920
921
922
923
924
925
926
927
928
929
930
931
932
933
934
935
936
937
938
939
940
941
942
943
944
945
946
947
948
949
950
951
952
953
954
955
956
957
958
959
960
961
962
963
964
965
966
967
968
969
970
971
972
973
974
975
976
977
978
979
980
981
982
983
984
985
986
987
988
989
990
991
992
993
994
995
996
997
998
999
1000
HEADER TRANSFERASE 02-SEP-02 1MLZ
TITLE CRYSTAL STRUCTURE OF 7,8-DIAMINOPELARGONIC ACID SYNTHASE IN COMPLEX
TITLE 2 WITH THE TRANS-ISOMER OF AMICLENOMYCIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 7,8-DIAMINO-PELARGONIC ACID AMINOTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE,
COMPND 5 DAPA AMINOTRANSFERASE;
COMPND 6 EC: 2.6.1.62;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: BIOA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET24
KEYWDS AMINOTRANSFERASE, FOLD TYPE I, SUBCLASS II, AMICLENOMYCIN,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SANDMARK,S.MANN,A.MARQUET,G.SCHNEIDER
REVDAT 4 07-MAR-18 1MLZ 1 REMARK
REVDAT 3 13-JUL-11 1MLZ 1 VERSN
REVDAT 2 24-FEB-09 1MLZ 1 VERSN
REVDAT 1 04-DEC-02 1MLZ 0
JRNL AUTH J.SANDMARK,S.MANN,A.MARQUET,G.SCHNEIDER
JRNL TITL STRUCTURAL BASIS FOR THE INHIBITION OF THE BIOSYNTHESIS OF
JRNL TITL 2 BIOTIN BY THE ANTIBIOTIC AMICLENOMYCIN
JRNL REF J.BIOL.CHEM. V. 277 43352 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12218056
JRNL DOI 10.1074/JBC.M207239200
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 39635
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2108
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2696
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 158
REMARK 3 BIN FREE R VALUE : 0.3790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6587
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 324
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.28000
REMARK 3 B22 (A**2) : 2.67000
REMARK 3 B33 (A**2) : -2.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.69000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.334
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.219
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.237
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.138
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6638 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 6097 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9002 ; 1.583 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14057 ; 1.898 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 836 ; 3.937 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1132 ;18.550 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 999 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7386 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1364 ; 0.026 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1581 ; 0.273 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5924 ; 0.221 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 13 ; 0.289 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 423 ; 0.174 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 7 ; 0.178 ; 0.500
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 13 ; 0.250 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 43 ; 0.245 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.401 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4209 ; 0.677 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6714 ; 1.260 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2429 ; 1.795 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2288 ; 2.917 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 IN MONOMER A TWO STRETCHES OF RESIDUES ARE DISORDERED, 159-169 AND
REMARK 3 186-192 RESP.
REMARK 3 IN MONOMER B THREE STRETCHES OF RESIDUES ARE DISORDERED, 158-168,
REMARK 3 189-194 AND 296-301 RESP.
REMARK 3 RESIDUE 429 WAS EXCLUDED FROM BOTH MONOMERS. A NUMBER OF
REMARK 3 SIDECHAINS ON THE SURFACE OF THE
REMARK 3 PROTEIN ARE DISORDERED. THE OCCUPANCY FOR THESE IS ESTIMATED TO 0
REMARK 3 IN MOST CASES.
REMARK 4
REMARK 4 1MLZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-02.
REMARK 100 THE DEPOSITION ID IS D_1000017006.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.991
REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41748
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 22.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.29100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, MPD, HEPES, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 64.01700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.98000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.01700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.98000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -110.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 183
REMARK 465 GLN A 429
REMARK 465 GLN B 429
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 TRP B 53 NE1
REMARK 470 GLU B 185 CG CD OE1 OE2
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 PRO A 23
REMARK 475 VAL A 192
REMARK 475 HIS A 203
REMARK 475 ASP A 423
REMARK 475 VAL B 30
REMARK 475 ALA B 133
REMARK 475 ASP B 183
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 SER A 22 OG
REMARK 480 GLN A 101 CB CG CD OE1 NE2
REMARK 480 GLN A 128 CD OE1 NE2
REMARK 480 ALA A 133 CB
REMARK 480 ARG A 141 CD NE CZ NH1 NH2
REMARK 480 LEU A 164 CB CG CD1 CD2
REMARK 480 GLU A 171 CD OE1 OE2
REMARK 480 GLU A 185 CD OE1 OE2
REMARK 480 ARG A 189 CB CG CD NE CZ NH1 NH2
REMARK 480 ASP A 190 CG OD1 OD2
REMARK 480 ARG A 196 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG A 202 CZ NH1 NH2
REMARK 480 GLU A 264 CG CD OE1 OE2
REMARK 480 GLU A 300 CD OE1 OE2
REMARK 480 GLU A 328 CD OE1 OE2
REMARK 480 GLN A 334 CD OE1 NE2
REMARK 480 GLU A 354 CD OE1 OE2
REMARK 480 LYS A 381 CE NZ
REMARK 480 GLU A 385 CD OE1 OE2
REMARK 480 GLU A 424 CG CD OE1 OE2
REMARK 480 SER B 22 OG
REMARK 480 GLU B 33 CD OE1 OE2
REMARK 480 GLN B 63 CD OE1 NE2
REMARK 480 GLU B 90 CD OE1 OE2
REMARK 480 GLN B 101 CB CG CD OE1 NE2
REMARK 480 GLN B 135 CG CD OE1 NE2
REMARK 480 ASP B 158 CB CG OD1 OD2
REMARK 480 LYS B 166 CE NZ
REMARK 480 GLU B 171 CD OE1 OE2
REMARK 480 ASP B 187 CB CG OD1 OD2
REMARK 480 ARG B 202 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS B 233 CA CB
REMARK 480 ARG B 237 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU B 300 CD OE1 OE2
REMARK 480 GLN B 334 CB CG CD OE1 NE2
REMARK 480 ASP B 338 CB CG OD1 OD2
REMARK 480 GLU B 345 CD OE1 OE2
REMARK 480 ASP B 352 CG OD1 OD2
REMARK 480 MET B 355 CG SD CE
REMARK 480 LYS B 381 CE NZ
REMARK 480 GLU B 424 CD OE1 OE2
REMARK 480 CYS B 428 CB SG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP A 423 O HOH A 4090 1.71
REMARK 500 O ASP A 423 N GLU A 424 1.73
REMARK 500 OE2 GLU A 188 NH2 ARG A 230 1.81
REMARK 500 OD1 ASP B 423 OG1 THR B 425 1.85
REMARK 500 OH TYR B 17 OD1 ASP B 147 1.97
REMARK 500 OD2 ASP A 41 NH1 ARG A 43 2.13
REMARK 500 O3P PLP B 530 O HOH B 4128 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS A 381 O HOH A 3018 2656 0.62
REMARK 500 O THR B 21 O THR B 21 2655 1.48
REMARK 500 O HOH B 4038 O HOH B 4038 2655 1.83
REMARK 500 CE LYS A 381 O HOH A 3018 2656 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 300 CG GLU A 300 CD 0.095
REMARK 500 GLU A 385 CG GLU A 385 CD 0.209
REMARK 500 ASP A 423 C GLU A 424 N 0.167
REMARK 500 TRP B 53 CA TRP B 53 CB -0.144
REMARK 500 TRP B 53 CB TRP B 53 CG 0.141
REMARK 500 TRP B 53 CG TRP B 53 CD1 0.351
REMARK 500 TRP B 53 CG TRP B 53 CD1 -0.189
REMARK 500 TRP B 53 CE3 TRP B 53 CZ3 0.105
REMARK 500 GLU B 90 CG GLU B 90 CD 0.161
REMARK 500 ARG B 189 CG ARG B 189 CD -0.170
REMARK 500 CYS B 428 CA CYS B 428 CB -0.115
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 110 CB - CG - OD1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 ASP A 190 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ASP A 190 CB - CG - OD1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP A 190 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP A 268 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 358 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 GLN A 422 CA - C - N ANGL. DEV. = -34.1 DEGREES
REMARK 500 GLN A 422 O - C - N ANGL. DEV. = 34.5 DEGREES
REMARK 500 ASP A 423 O - C - N ANGL. DEV. = -45.2 DEGREES
REMARK 500 GLU A 424 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 ASP B 4 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP B 53 CB - CG - CD2 ANGL. DEV. = -9.3 DEGREES
REMARK 500 TRP B 53 CD1 - CG - CD2 ANGL. DEV. = 13.8 DEGREES
REMARK 500 TRP B 53 CD1 - CG - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 TRP B 53 CE3 - CZ3 - CH2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASP B 110 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 PHE B 140 CB - CA - C ANGL. DEV. = -13.7 DEGREES
REMARK 500 ASP B 147 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 268 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP B 358 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP B 423 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 23 151.94 -43.79
REMARK 500 TRP A 53 -11.77 80.16
REMARK 500 MET A 75 120.33 175.78
REMARK 500 PRO A 100 150.48 -48.64
REMARK 500 ILE A 213 -48.77 74.33
REMARK 500 LYS A 274 -90.97 34.63
REMARK 500 ASN A 313 114.65 -39.06
REMARK 500 ALA A 364 45.50 -94.61
REMARK 500 GLU A 424 -21.55 -23.73
REMARK 500 TRP B 52 63.74 64.50
REMARK 500 TRP B 53 -29.52 77.25
REMARK 500 MET B 75 124.27 -179.56
REMARK 500 PRO B 100 134.06 -38.73
REMARK 500 ILE B 213 -50.85 66.87
REMARK 500 LYS B 274 -98.74 41.69
REMARK 500 ASN B 313 112.50 -31.53
REMARK 500 ALA B 364 43.86 -99.05
REMARK 500 MET B 400 73.29 -150.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 422 ASP A 423 -147.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASP A 423 41.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 A COVALENT ADDUCT IS FORMED BETWEEN PYRIDOXAL-5'-PHOSPHATE
REMARK 600 AND THE AMICLENOMYCIN IN THE A SUBUNIT. IN THE B SUBUNIT
REMARK 600 THE DENSITY FOR AMICLENOMYCIN IS SIGNIFICANTLY WEAKER.
REMARK 600 THE AMICLENOMYCIN MOLECULE IS MODELED AS NON-COVALENTLY
REMARK 600 BOUND IN THE B SUBUNIT, BUT THE MODEL HAS HIGH B FACTORS
REMARK 600 AND IS NOT WELL SUPPORTED BY STRUCTURAL DATA. FOR A BETTER
REMARK 600 VIEW OF THE PYRIDOXAL-5'-PHOSPHATE-AMICLENOMYCIN ADDUCT
REMARK 600 SEE THE A SUBUNIT IN THE STRUCTURE OF THE ENZYME IN
REMARK 600 COMPLEX WITH THE CIS-ISOMER (PDB ID 1MLY). FOR DETAILS
REMARK 600 SEE THE PRIMARY CITATION.
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PLP B 530
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 103 O
REMARK 620 2 VAL A 96 O 118.2
REMARK 620 3 PRO A 100 O 101.5 140.0
REMARK 620 4 THR A 99 O 157.4 78.2 62.2
REMARK 620 5 THR A 99 OG1 92.4 76.7 98.1 75.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 502 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU B 103 O
REMARK 620 2 VAL B 96 O 123.7
REMARK 620 3 THR B 99 OG1 103.5 85.3
REMARK 620 4 THR B 99 O 154.2 81.8 72.5
REMARK 620 5 PRO B 100 O 90.8 144.2 96.8 65.0
REMARK 620 6 HOH B2057 O 84.1 85.5 170.3 103.3 89.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TZA A 431
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TZA B 531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 430
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 530
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QJ5 RELATED DB: PDB
REMARK 900 WT STRUCTURE OF THE SAME ENZYME
REMARK 900 RELATED ID: 1DTY RELATED DB: PDB
REMARK 900 WT STRUCTURE OF THE SAME ENZYME
REMARK 900 RELATED ID: 1QJ3 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE SUBSTRATE COMPLEX WITH THE WT ENZYME
REMARK 900 RELATED ID: 1MGV RELATED DB: PDB
REMARK 900 R391A MUTANT OF THE SAME ENZYME
REMARK 900 RELATED ID: 1MLY RELATED DB: PDB
REMARK 900 1MLY CONTAINS THE SAME ENZYME COMPLEXED WITH THE CIS-ISOMER OF
REMARK 900 AMICLENOMYCIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CRYSTALLIZED PROTEIN DIFFERS FROM THE SWISSPROT
REMARK 999 SEQUENCE AT RESIDUE 14. NUMBER 14 IS A LEUCIN, WHILE
REMARK 999 IN THE SWISSPROT SEQUENCE NUMBER 14 IS A TRYPTOPHAN.
REMARK 999 THIS IS CONFIRMED BY DNA SEQUENCING AND WAS ALSO
REMARK 999 REPORTED FOR THE ORIGINAL WT STRUCTURE (1QJ5).
DBREF 1MLZ A 1 429 UNP P12995 BIOA_ECOLI 1 429
DBREF 1MLZ B 1 429 UNP P12995 BIOA_ECOLI 1 429
SEQADV 1MLZ LEU A 14 UNP P12995 TRP 14 SEE REMARK 999
SEQADV 1MLZ LEU B 14 UNP P12995 TRP 14 SEE REMARK 999
SEQRES 1 A 429 MET THR THR ASP ASP LEU ALA PHE ASP GLN ARG HIS ILE
SEQRES 2 A 429 LEU HIS PRO TYR THR SER MET THR SER PRO LEU PRO VAL
SEQRES 3 A 429 TYR PRO VAL VAL SER ALA GLU GLY CYS GLU LEU ILE LEU
SEQRES 4 A 429 SER ASP GLY ARG ARG LEU VAL ASP GLY MET SER SER TRP
SEQRES 5 A 429 TRP ALA ALA ILE HIS GLY TYR ASN HIS PRO GLN LEU ASN
SEQRES 6 A 429 ALA ALA MET LYS SER GLN ILE ASP ALA MET SER HIS VAL
SEQRES 7 A 429 MET PHE GLY GLY ILE THR HIS ALA PRO ALA ILE GLU LEU
SEQRES 8 A 429 CYS ARG LYS LEU VAL ALA MET THR PRO GLN PRO LEU GLU
SEQRES 9 A 429 CYS VAL PHE LEU ALA ASP SER GLY SER VAL ALA VAL GLU
SEQRES 10 A 429 VAL ALA MET LYS MET ALA LEU GLN TYR TRP GLN ALA LYS
SEQRES 11 A 429 GLY GLU ALA ARG GLN ARG PHE LEU THR PHE ARG ASN GLY
SEQRES 12 A 429 TYR HIS GLY ASP THR PHE GLY ALA MET SER VAL CYS ASP
SEQRES 13 A 429 PRO ASP ASN SER MET HIS SER LEU TRP LYS GLY TYR LEU
SEQRES 14 A 429 PRO GLU ASN LEU PHE ALA PRO ALA PRO GLN SER ARG MET
SEQRES 15 A 429 ASP GLY GLU TRP ASP GLU ARG ASP MET VAL GLY PHE ALA
SEQRES 16 A 429 ARG LEU MET ALA ALA HIS ARG HIS GLU ILE ALA ALA VAL
SEQRES 17 A 429 ILE ILE GLU PRO ILE VAL GLN GLY ALA GLY GLY MET ARG
SEQRES 18 A 429 MET TYR HIS PRO GLU TRP LEU LYS ARG ILE ARG LYS ILE
SEQRES 19 A 429 CYS ASP ARG GLU GLY ILE LEU LEU ILE ALA ASP GLU ILE
SEQRES 20 A 429 ALA THR GLY PHE GLY ARG THR GLY LYS LEU PHE ALA CYS
SEQRES 21 A 429 GLU HIS ALA GLU ILE ALA PRO ASP ILE LEU CYS LEU GLY
SEQRES 22 A 429 LYS ALA LEU THR GLY GLY THR MET THR LEU SER ALA THR
SEQRES 23 A 429 LEU THR THR ARG GLU VAL ALA GLU THR ILE SER ASN GLY
SEQRES 24 A 429 GLU ALA GLY CYS PHE MET HIS GLY PRO THR PHE MET GLY
SEQRES 25 A 429 ASN PRO LEU ALA CYS ALA ALA ALA ASN ALA SER LEU ALA
SEQRES 26 A 429 ILE LEU GLU SER GLY ASP TRP GLN GLN GLN VAL ALA ASP
SEQRES 27 A 429 ILE GLU VAL GLN LEU ARG GLU GLN LEU ALA PRO ALA ARG
SEQRES 28 A 429 ASP ALA GLU MET VAL ALA ASP VAL ARG VAL LEU GLY ALA
SEQRES 29 A 429 ILE GLY VAL VAL GLU THR THR HIS PRO VAL ASN MET ALA
SEQRES 30 A 429 ALA LEU GLN LYS PHE PHE VAL GLU GLN GLY VAL TRP ILE
SEQRES 31 A 429 ARG PRO PHE GLY LYS LEU ILE TYR LEU MET PRO PRO TYR
SEQRES 32 A 429 ILE ILE LEU PRO GLN GLN LEU GLN ARG LEU THR ALA ALA
SEQRES 33 A 429 VAL ASN ARG ALA VAL GLN ASP GLU THR PHE PHE CYS GLN
SEQRES 1 B 429 MET THR THR ASP ASP LEU ALA PHE ASP GLN ARG HIS ILE
SEQRES 2 B 429 LEU HIS PRO TYR THR SER MET THR SER PRO LEU PRO VAL
SEQRES 3 B 429 TYR PRO VAL VAL SER ALA GLU GLY CYS GLU LEU ILE LEU
SEQRES 4 B 429 SER ASP GLY ARG ARG LEU VAL ASP GLY MET SER SER TRP
SEQRES 5 B 429 TRP ALA ALA ILE HIS GLY TYR ASN HIS PRO GLN LEU ASN
SEQRES 6 B 429 ALA ALA MET LYS SER GLN ILE ASP ALA MET SER HIS VAL
SEQRES 7 B 429 MET PHE GLY GLY ILE THR HIS ALA PRO ALA ILE GLU LEU
SEQRES 8 B 429 CYS ARG LYS LEU VAL ALA MET THR PRO GLN PRO LEU GLU
SEQRES 9 B 429 CYS VAL PHE LEU ALA ASP SER GLY SER VAL ALA VAL GLU
SEQRES 10 B 429 VAL ALA MET LYS MET ALA LEU GLN TYR TRP GLN ALA LYS
SEQRES 11 B 429 GLY GLU ALA ARG GLN ARG PHE LEU THR PHE ARG ASN GLY
SEQRES 12 B 429 TYR HIS GLY ASP THR PHE GLY ALA MET SER VAL CYS ASP
SEQRES 13 B 429 PRO ASP ASN SER MET HIS SER LEU TRP LYS GLY TYR LEU
SEQRES 14 B 429 PRO GLU ASN LEU PHE ALA PRO ALA PRO GLN SER ARG MET
SEQRES 15 B 429 ASP GLY GLU TRP ASP GLU ARG ASP MET VAL GLY PHE ALA
SEQRES 16 B 429 ARG LEU MET ALA ALA HIS ARG HIS GLU ILE ALA ALA VAL
SEQRES 17 B 429 ILE ILE GLU PRO ILE VAL GLN GLY ALA GLY GLY MET ARG
SEQRES 18 B 429 MET TYR HIS PRO GLU TRP LEU LYS ARG ILE ARG LYS ILE
SEQRES 19 B 429 CYS ASP ARG GLU GLY ILE LEU LEU ILE ALA ASP GLU ILE
SEQRES 20 B 429 ALA THR GLY PHE GLY ARG THR GLY LYS LEU PHE ALA CYS
SEQRES 21 B 429 GLU HIS ALA GLU ILE ALA PRO ASP ILE LEU CYS LEU GLY
SEQRES 22 B 429 LYS ALA LEU THR GLY GLY THR MET THR LEU SER ALA THR
SEQRES 23 B 429 LEU THR THR ARG GLU VAL ALA GLU THR ILE SER ASN GLY
SEQRES 24 B 429 GLU ALA GLY CYS PHE MET HIS GLY PRO THR PHE MET GLY
SEQRES 25 B 429 ASN PRO LEU ALA CYS ALA ALA ALA ASN ALA SER LEU ALA
SEQRES 26 B 429 ILE LEU GLU SER GLY ASP TRP GLN GLN GLN VAL ALA ASP
SEQRES 27 B 429 ILE GLU VAL GLN LEU ARG GLU GLN LEU ALA PRO ALA ARG
SEQRES 28 B 429 ASP ALA GLU MET VAL ALA ASP VAL ARG VAL LEU GLY ALA
SEQRES 29 B 429 ILE GLY VAL VAL GLU THR THR HIS PRO VAL ASN MET ALA
SEQRES 30 B 429 ALA LEU GLN LYS PHE PHE VAL GLU GLN GLY VAL TRP ILE
SEQRES 31 B 429 ARG PRO PHE GLY LYS LEU ILE TYR LEU MET PRO PRO TYR
SEQRES 32 B 429 ILE ILE LEU PRO GLN GLN LEU GLN ARG LEU THR ALA ALA
SEQRES 33 B 429 VAL ASN ARG ALA VAL GLN ASP GLU THR PHE PHE CYS GLN
HET TZA A 431 14
HET NA A 501 1
HET PLP A 430 15
HET TZA B 531 14
HET NA B 502 1
HET PLP B 530 15
HETNAM TZA TRANS-AMICLENOMYCIN
HETNAM NA SODIUM ION
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN TZA 2-AMINO-4-(4-AMINO-CYCLOHEXA-2,5-DIENYL)-BUTYRIC ACID
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 TZA 2(C10 H16 N2 O2)
FORMUL 4 NA 2(NA 1+)
FORMUL 5 PLP 2(C8 H10 N O6 P)
FORMUL 9 HOH *324(H2 O)
HELIX 1 1 THR A 2 ILE A 13 1 12
HELIX 2 2 HIS A 61 MET A 75 1 15
HELIX 3 3 HIS A 85 THR A 99 1 15
HELIX 4 4 SER A 111 LYS A 130 1 20
HELIX 5 5 THR A 148 SER A 153 1 6
HELIX 6 6 MET A 161 LYS A 166 5 6
HELIX 7 7 ASP A 187 ASP A 190 5 4
HELIX 8 8 MET A 191 ARG A 202 1 12
HELIX 9 9 PRO A 225 GLY A 239 1 15
HELIX 10 10 PHE A 258 GLU A 264 5 7
HELIX 11 11 GLY A 273 GLY A 278 5 6
HELIX 12 12 THR A 289 ASN A 298 1 10
HELIX 13 13 ASN A 313 SER A 329 1 17
HELIX 14 14 ASP A 331 ALA A 348 1 18
HELIX 15 15 PRO A 349 ALA A 353 5 5
HELIX 16 16 ASN A 375 GLN A 386 1 12
HELIX 17 17 LEU A 406 VAL A 421 1 16
HELIX 18 18 THR B 2 ILE B 13 1 12
HELIX 19 19 HIS B 61 MET B 75 1 15
HELIX 20 20 HIS B 85 THR B 99 1 15
HELIX 21 21 SER B 111 GLY B 131 1 21
HELIX 22 22 THR B 148 SER B 153 1 6
HELIX 23 23 MET B 161 TRP B 165 5 5
HELIX 24 24 MET B 191 ARG B 202 1 12
HELIX 25 25 PRO B 225 GLY B 239 1 15
HELIX 26 26 PHE B 258 ALA B 263 5 6
HELIX 27 27 GLY B 273 GLY B 278 5 6
HELIX 28 28 ARG B 290 ASN B 298 1 9
HELIX 29 29 ASN B 313 SER B 329 1 17
HELIX 30 30 GLY B 330 ALA B 348 1 19
HELIX 31 31 PRO B 349 ALA B 353 5 5
HELIX 32 32 ASN B 375 GLN B 386 1 12
HELIX 33 33 LEU B 406 VAL B 421 1 16
HELIX 34 34 GLN B 422 PHE B 427 5 6
SHEET 1 A 5 VAL A 388 TRP A 389 0
SHEET 2 A 5 ARG A 44 ASP A 47 1 N VAL A 46 O TRP A 389
SHEET 3 A 5 GLU A 36 LEU A 39 -1 N LEU A 37 O LEU A 45
SHEET 4 A 5 TYR A 27 GLU A 33 -1 N SER A 31 O ILE A 38
SHEET 5 A 5 ILE B 83 THR B 84 1 O THR B 84 N TYR A 27
SHEET 1 B 5 ILE A 83 THR A 84 0
SHEET 2 B 5 TYR B 27 GLU B 33 1 O VAL B 29 N THR A 84
SHEET 3 B 5 GLU B 36 LEU B 39 -1 O ILE B 38 N SER B 31
SHEET 4 B 5 ARG B 44 ASP B 47 -1 O LEU B 45 N LEU B 37
SHEET 5 B 5 VAL B 388 TRP B 389 1 O TRP B 389 N VAL B 46
SHEET 1 C 7 CYS A 105 ALA A 109 0
SHEET 2 C 7 SER A 284 THR A 288 -1 O SER A 284 N ALA A 109
SHEET 3 C 7 ILE A 269 LEU A 272 -1 N LEU A 272 O ALA A 285
SHEET 4 C 7 LEU A 241 ASP A 245 1 N ALA A 244 O ILE A 269
SHEET 5 C 7 ILE A 205 ILE A 210 1 N VAL A 208 O ILE A 243
SHEET 6 C 7 ARG A 136 PHE A 140 1 N LEU A 138 O ILE A 209
SHEET 7 C 7 LEU A 173 ALA A 175 1 O ALA A 175 N THR A 139
SHEET 1 D 2 VAL A 214 GLN A 215 0
SHEET 2 D 2 ARG A 221 MET A 222 -1 O ARG A 221 N GLN A 215
SHEET 1 E 3 VAL A 356 LEU A 362 0
SHEET 2 E 3 ILE A 365 THR A 370 -1 O VAL A 367 N ARG A 360
SHEET 3 E 3 LEU A 396 LEU A 399 -1 O LEU A 399 N GLY A 366
SHEET 1 F 7 LEU B 103 ALA B 109 0
SHEET 2 F 7 SER B 284 THR B 289 -1 O SER B 284 N ALA B 109
SHEET 3 F 7 ILE B 269 LEU B 272 -1 N LEU B 272 O ALA B 285
SHEET 4 F 7 LEU B 241 ASP B 245 1 N ALA B 244 O ILE B 269
SHEET 5 F 7 ILE B 205 ILE B 210 1 N VAL B 208 O ILE B 243
SHEET 6 F 7 ARG B 136 PHE B 140 1 N ARG B 136 O ALA B 206
SHEET 7 F 7 LEU B 173 ALA B 175 1 O LEU B 173 N THR B 139
SHEET 1 G 2 VAL B 214 GLN B 215 0
SHEET 2 G 2 ARG B 221 MET B 222 -1 O ARG B 221 N GLN B 215
SHEET 1 H 3 VAL B 356 LEU B 362 0
SHEET 2 H 3 ILE B 365 THR B 370 -1 O GLU B 369 N ASP B 358
SHEET 3 H 3 LEU B 396 LEU B 399 -1 O LEU B 399 N GLY B 366
LINK C4A PLP A 430 NH TZA A 431 1555 1555 1.46
LINK NA NA A 501 O LEU A 103 1555 1555 2.18
LINK NA NA A 501 O VAL A 96 1555 1555 2.37
LINK NA NA A 501 O PRO A 100 1555 1555 2.48
LINK NA NA B 502 O LEU B 103 1555 1555 2.16
LINK NA NA B 502 O VAL B 96 1555 1555 2.32
LINK NA NA B 502 OG1 THR B 99 1555 1555 2.55
LINK O THR A 99 NA NA A 501 1555 1555 2.92
LINK OG1 THR A 99 NA NA A 501 1555 1555 2.75
LINK O THR B 99 NA NA B 502 1555 1555 2.94
LINK O PRO B 100 NA NA B 502 1555 1555 2.65
LINK NA NA B 502 O HOH B2057 1555 1555 2.62
SITE 1 AC1 8 TRP A 52 TYR A 144 LYS A 274 ARG A 391
SITE 2 AC1 8 PHE A 393 PLP A 430 HOH A 432 HOH A 439
SITE 1 AC2 9 TRP B 52 TRP B 53 TYR B 144 ARG B 391
SITE 2 AC2 9 PHE B 393 PLP B 530 HOH B4034 HOH B4035
SITE 3 AC2 9 HOH B4081
SITE 1 AC3 4 VAL A 96 THR A 99 PRO A 100 LEU A 103
SITE 1 AC4 5 VAL B 96 THR B 99 PRO B 100 LEU B 103
SITE 2 AC4 5 HOH B2057
SITE 1 AC5 13 GLY A 112 SER A 113 TYR A 144 HIS A 145
SITE 2 AC5 13 ASP A 245 ILE A 247 LYS A 274 TZA A 431
SITE 3 AC5 13 HOH A 435 HOH A 443 HOH A4111 PRO B 308
SITE 4 AC5 13 THR B 309
SITE 1 AC6 15 PRO A 308 THR A 309 HOH A2004 TRP B 53
SITE 2 AC6 15 GLY B 112 SER B 113 HIS B 145 GLU B 211
SITE 3 AC6 15 ASP B 245 ILE B 247 LYS B 274 TZA B 531
SITE 4 AC6 15 HOH B2002 HOH B4017 HOH B4128
CRYST1 128.034 55.960 116.001 90.00 109.65 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007810 0.000000 0.002789 0.00000
SCALE2 0.000000 0.017870 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009154 0.00000
ATOM 1 N MET A 1 46.291 18.726 48.315 1.00 41.42 N
ATOM 2 CA MET A 1 45.520 17.458 48.351 1.00 41.12 C
ATOM 3 C MET A 1 44.881 17.292 49.723 1.00 40.44 C
ATOM 4 O MET A 1 45.555 17.150 50.724 1.00 40.41 O
ATOM 5 CB MET A 1 46.430 16.266 48.029 1.00 41.22 C
ATOM 6 CG MET A 1 46.717 16.092 46.539 1.00 41.96 C
ATOM 7 SD MET A 1 47.995 14.849 46.218 1.00 42.64 S
ATOM 8 CE MET A 1 49.384 15.803 46.567 1.00 39.42 C
ATOM 9 N THR A 2 43.585 17.493 49.758 1.00 39.93 N
ATOM 10 CA THR A 2 42.750 17.217 50.885 1.00 39.29 C
ATOM 11 C THR A 2 42.809 15.782 51.389 1.00 39.26 C
ATOM 12 O THR A 2 43.261 14.853 50.687 1.00 39.76 O
ATOM 13 CB THR A 2 41.328 17.508 50.465 1.00 39.25 C
ATOM 14 OG1 THR A 2 40.880 16.480 49.574 1.00 38.45 O
ATOM 15 CG2 THR A 2 41.237 18.787 49.639 1.00 39.33 C
ATOM 16 N THR A 3 42.315 15.597 52.609 1.00 37.87 N
ATOM 17 CA THR A 3 42.315 14.289 53.237 1.00 37.04 C
ATOM 18 C THR A 3 41.406 13.381 52.442 1.00 36.03 C
ATOM 19 O THR A 3 41.641 12.175 52.345 1.00 35.14 O
ATOM 20 CB THR A 3 41.849 14.368 54.696 1.00 36.89 C
ATOM 21 OG1 THR A 3 40.553 14.966 54.768 1.00 37.18 O
ATOM 22 CG2 THR A 3 42.721 15.292 55.487 1.00 37.20 C
ATOM 23 N ASP A 4 40.358 13.961 51.873 1.00 35.16 N
ATOM 24 CA ASP A 4 39.444 13.196 51.033 1.00 35.03 C
ATOM 25 C ASP A 4 40.082 12.753 49.696 1.00 34.57 C
ATOM 26 O ASP A 4 39.664 11.758 49.086 1.00 33.84 O
ATOM 27 CB ASP A 4 38.206 14.005 50.720 1.00 35.17 C
ATOM 28 CG ASP A 4 37.223 13.219 49.926 1.00 35.83 C
ATOM 29 OD1 ASP A 4 36.809 12.155 50.424 1.00 39.50 O
ATOM 30 OD2 ASP A 4 36.852 13.546 48.781 1.00 38.01 O
ATOM 31 N ASP A 5 41.050 13.532 49.223 1.00 34.49 N
ATOM 32 CA ASP A 5 41.798 13.183 48.022 1.00 34.06 C
ATOM 33 C ASP A 5 42.571 11.906 48.328 1.00 33.35 C
ATOM 34 O ASP A 5 42.549 10.947 47.567 1.00 33.58 O
ATOM 35 CB ASP A 5 42.773 14.292 47.650 1.00 34.29 C
ATOM 36 CG ASP A 5 42.112 15.457 46.947 1.00 34.27 C
ATOM 37 OD1 ASP A 5 41.016 15.298 46.376 1.00 35.62 O
ATOM 38 OD2 ASP A 5 42.630 16.584 46.913 1.00 33.99 O
ATOM 39 N LEU A 6 43.213 11.884 49.482 1.00 32.56 N
ATOM 40 CA LEU A 6 44.002 10.742 49.882 1.00 32.21 C
ATOM 41 C LEU A 6 43.142 9.525 50.155 1.00 31.67 C
ATOM 42 O LEU A 6 43.552 8.379 49.895 1.00 30.55 O
ATOM 43 CB LEU A 6 44.841 11.100 51.090 1.00 32.47 C
ATOM 44 CG LEU A 6 45.786 12.252 50.785 1.00 35.16 C
ATOM 45 CD1 LEU A 6 46.571 12.512 52.034 1.00 38.66 C
ATOM 46 CD2 LEU A 6 46.743 11.971 49.628 1.00 37.24 C
ATOM 47 N ALA A 7 41.945 9.770 50.680 1.00 31.14 N
ATOM 48 CA ALA A 7 40.993 8.703 50.900 1.00 30.49 C
ATOM 49 C ALA A 7 40.639 8.071 49.581 1.00 29.67 C
ATOM 50 O ALA A 7 40.575 6.848 49.460 1.00 30.39 O
ATOM 51 CB ALA A 7 39.723 9.235 51.575 1.00 30.68 C
ATOM 52 N PHE A 8 40.365 8.906 48.592 1.00 28.73 N
ATOM 53 CA PHE A 8 39.998 8.407 47.287 1.00 27.90 C
ATOM 54 C PHE A 8 41.113 7.544 46.681 1.00 27.02 C
ATOM 55 O PHE A 8 40.846 6.469 46.150 1.00 26.54 O
ATOM 56 CB PHE A 8 39.614 9.532 46.339 1.00 27.92 C
ATOM 57 CG PHE A 8 39.133 9.027 45.014 1.00 27.61 C
ATOM 58 CD1 PHE A 8 40.034 8.786 44.000 1.00 28.51 C
ATOM 59 CD2 PHE A 8 37.805 8.760 44.799 1.00 25.44 C
ATOM 60 CE1 PHE A 8 39.623 8.307 42.829 1.00 27.73 C
ATOM 61 CE2 PHE A 8 37.395 8.284 43.618 1.00 25.06 C
ATOM 62 CZ PHE A 8 38.298 8.049 42.629 1.00 27.33 C
ATOM 63 N ASP A 9 42.352 8.005 46.802 1.00 26.52 N
ATOM 64 CA ASP A 9 43.497 7.290 46.247 1.00 26.27 C
ATOM 65 C ASP A 9 43.517 5.896 46.850 1.00 26.56 C
ATOM 66 O ASP A 9 43.499 4.892 46.136 1.00 25.13 O
ATOM 67 CB ASP A 9 44.796 8.041 46.559 1.00 26.03 C
ATOM 68 CG ASP A 9 46.036 7.242 46.228 1.00 26.31 C
ATOM 69 OD1 ASP A 9 46.571 7.283 45.085 1.00 25.86 O
ATOM 70 OD2 ASP A 9 46.563 6.541 47.139 1.00 24.69 O
ATOM 71 N GLN A 10 43.486 5.853 48.177 1.00 27.36 N
ATOM 72 CA GLN A 10 43.582 4.608 48.911 1.00 28.85 C
ATOM 73 C GLN A 10 42.498 3.627 48.509 1.00 29.00 C
ATOM 74 O GLN A 10 42.779 2.465 48.331 1.00 29.19 O
ATOM 75 CB GLN A 10 43.557 4.864 50.436 1.00 29.70 C
ATOM 76 CG GLN A 10 43.708 3.601 51.277 1.00 30.84 C
ATOM 77 CD GLN A 10 43.753 3.871 52.764 1.00 34.28 C
ATOM 78 OE1 GLN A 10 42.725 3.825 53.438 1.00 36.79 O
ATOM 79 NE2 GLN A 10 44.946 4.126 53.286 1.00 36.67 N
ATOM 80 N ARG A 11 41.262 4.084 48.346 1.00 30.19 N
ATOM 81 CA ARG A 11 40.172 3.156 48.011 1.00 31.02 C
ATOM 82 C ARG A 11 39.954 2.885 46.543 1.00 30.15 C
ATOM 83 O ARG A 11 39.406 1.830 46.197 1.00 29.75 O
ATOM 84 CB ARG A 11 38.831 3.595 48.632 1.00 31.92 C
ATOM 85 CG ARG A 11 38.645 3.095 50.090 1.00 36.94 C
ATOM 86 CD ARG A 11 37.222 2.629 50.451 1.00 41.19 C
ATOM 87 NE ARG A 11 37.212 1.192 50.705 1.00 44.41 N
ATOM 88 CZ ARG A 11 36.328 0.341 50.230 1.00 46.86 C
ATOM 89 NH1 ARG A 11 35.323 0.770 49.483 1.00 48.28 N
ATOM 90 NH2 ARG A 11 36.452 -0.957 50.516 1.00 48.86 N
ATOM 91 N HIS A 12 40.403 3.795 45.689 1.00 28.98 N
ATOM 92 CA HIS A 12 40.080 3.714 44.273 1.00 28.76 C
ATOM 93 C HIS A 12 41.229 3.599 43.303 1.00 27.47 C
ATOM 94 O HIS A 12 41.009 3.234 42.166 1.00 28.27 O
ATOM 95 CB HIS A 12 39.238 4.927 43.905 1.00 29.20 C
ATOM 96 CG HIS A 12 37.910 4.931 44.587 1.00 31.27 C
ATOM 97 ND1 HIS A 12 36.917 4.024 44.275 1.00 32.99 N
ATOM 98 CD2 HIS A 12 37.434 5.675 45.609 1.00 31.92 C
ATOM 99 CE1 HIS A 12 35.867 4.245 45.048 1.00 32.62 C
ATOM 100 NE2 HIS A 12 36.157 5.235 45.869 1.00 33.43 N
ATOM 101 N ILE A 13 42.444 3.881 43.745 1.00 26.27 N
ATOM 102 CA ILE A 13 43.614 3.867 42.851 1.00 25.06 C
ATOM 103 C ILE A 13 44.556 2.729 43.163 1.00 24.56 C
ATOM 104 O ILE A 13 45.108 2.651 44.251 1.00 23.44 O
ATOM 105 CB ILE A 13 44.354 5.219 42.929 1.00 24.02 C
ATOM 106 CG1 ILE A 13 43.359 6.341 42.649 1.00 23.44 C
ATOM 107 CG2 ILE A 13 45.495 5.250 41.946 1.00 23.66 C
ATOM 108 CD1 ILE A 13 43.949 7.763 42.579 1.00 23.29 C
ATOM 109 N LEU A 14 44.749 1.860 42.179 1.00 25.87 N
ATOM 110 CA LEU A 14 45.661 0.756 42.334 1.00 27.06 C
ATOM 111 C LEU A 14 47.040 1.311 42.154 1.00 26.95 C
ATOM 112 O LEU A 14 47.303 2.132 41.272 1.00 27.87 O
ATOM 113 CB LEU A 14 45.383 -0.370 41.355 1.00 27.55 C
ATOM 114 CG LEU A 14 44.374 -1.387 41.871 1.00 30.15 C
ATOM 115 CD1 LEU A 14 43.012 -0.863 41.597 1.00 31.52 C
ATOM 116 CD2 LEU A 14 44.547 -2.769 41.222 1.00 31.86 C
ATOM 117 N HIS A 15 47.900 0.911 43.039 1.00 26.84 N
ATOM 118 CA HIS A 15 49.252 1.322 43.020 1.00 27.06 C
ATOM 119 C HIS A 15 50.045 0.077 42.643 1.00 28.84 C
ATOM 120 O HIS A 15 49.537 -1.037 42.688 1.00 28.87 O
ATOM 121 CB HIS A 15 49.623 1.932 44.350 1.00 26.64 C
ATOM 122 CG HIS A 15 49.247 3.379 44.456 1.00 25.76 C
ATOM 123 ND1 HIS A 15 50.143 4.406 44.226 1.00 24.17 N
ATOM 124 CD2 HIS A 15 48.056 3.972 44.720 1.00 25.68 C
ATOM 125 CE1 HIS A 15 49.516 5.566 44.349 1.00 26.48 C
ATOM 126 NE2 HIS A 15 48.254 5.333 44.664 1.00 23.66 N
ATOM 127 N PRO A 16 51.273 0.254 42.207 1.00 30.50 N
ATOM 128 CA PRO A 16 52.060 -0.880 41.725 1.00 31.68 C
ATOM 129 C PRO A 16 52.362 -1.911 42.794 1.00 32.69 C
ATOM 130 O PRO A 16 52.806 -1.560 43.885 1.00 32.67 O
ATOM 131 CB PRO A 16 53.392 -0.242 41.248 1.00 31.42 C
ATOM 132 CG PRO A 16 53.288 1.201 41.448 1.00 30.98 C
ATOM 133 CD PRO A 16 52.009 1.525 42.158 1.00 30.99 C
ATOM 134 N TYR A 17 52.163 -3.171 42.438 1.00 34.36 N
ATOM 135 CA TYR A 17 52.524 -4.310 43.274 1.00 36.15 C
ATOM 136 C TYR A 17 52.151 -4.099 44.713 1.00 37.07 C
ATOM 137 O TYR A 17 52.945 -4.349 45.613 1.00 37.72 O
ATOM 138 CB TYR A 17 54.016 -4.628 43.138 1.00 36.43 C
ATOM 139 CG TYR A 17 54.283 -5.323 41.817 1.00 36.70 C
ATOM 140 CD1 TYR A 17 54.060 -6.690 41.660 1.00 37.44 C
ATOM 141 CD2 TYR A 17 54.693 -4.598 40.715 1.00 35.52 C
ATOM 142 CE1 TYR A 17 54.272 -7.299 40.426 1.00 37.70 C
ATOM 143 CE2 TYR A 17 54.907 -5.192 39.506 1.00 34.96 C
ATOM 144 CZ TYR A 17 54.690 -6.535 39.354 1.00 36.72 C
ATOM 145 OH TYR A 17 54.894 -7.109 38.119 1.00 36.62 O
ATOM 146 N THR A 18 50.939 -3.618 44.929 1.00 38.41 N
ATOM 147 CA THR A 18 50.502 -3.395 46.275 1.00 39.76 C
ATOM 148 C THR A 18 49.020 -3.609 46.407 1.00 40.53 C
ATOM 149 O THR A 18 48.261 -3.351 45.496 1.00 41.04 O
ATOM 150 CB THR A 18 50.873 -2.020 46.753 1.00 40.06 C
ATOM 151 OG1 THR A 18 50.538 -1.931 48.153 1.00 42.43 O
ATOM 152 CG2 THR A 18 50.046 -0.985 46.096 1.00 39.19 C
ATOM 153 N SER A 19 48.626 -4.065 47.584 1.00 41.59 N
ATOM 154 CA SER A 19 47.256 -4.460 47.851 1.00 42.05 C
ATOM 155 C SER A 19 46.212 -3.337 47.916 1.00 43.31 C
ATOM 156 O SER A 19 46.465 -2.224 48.373 1.00 42.37 O
ATOM 157 CB SER A 19 47.221 -5.214 49.170 1.00 41.97 C
ATOM 158 OG SER A 19 45.895 -5.363 49.611 1.00 40.88 O
ATOM 159 N MET A 20 45.017 -3.683 47.450 1.00 44.54 N
ATOM 160 CA MET A 20 43.860 -2.826 47.582 1.00 45.61 C
ATOM 161 C MET A 20 43.079 -3.057 48.885 1.00 46.12 C
ATOM 162 O MET A 20 42.218 -2.259 49.231 1.00 46.55 O
ATOM 163 CB MET A 20 42.961 -3.030 46.384 1.00 45.67 C
ATOM 164 CG MET A 20 43.504 -2.327 45.175 1.00 47.51 C
ATOM 165 SD MET A 20 43.505 -0.517 45.429 1.00 49.67 S
ATOM 166 CE MET A 20 41.856 -0.191 45.067 1.00 46.83 C
ATOM 167 N THR A 21 43.439 -4.075 49.655 1.00 46.80 N
ATOM 168 CA THR A 21 42.712 -4.382 50.895 1.00 47.59 C
ATOM 169 C THR A 21 43.468 -3.948 52.154 1.00 48.04 C
ATOM 170 O THR A 21 42.855 -3.540 53.136 1.00 47.94 O
ATOM 171 CB THR A 21 42.392 -5.895 50.993 1.00 47.24 C
ATOM 172 OG1 THR A 21 43.594 -6.670 50.995 1.00 46.77 O
ATOM 173 CG2 THR A 21 41.651 -6.383 49.763 1.00 48.32 C
ATOM 174 N SER A 22 44.792 -4.083 52.120 1.00 48.74 N
ATOM 175 CA SER A 22 45.659 -3.793 53.255 1.00 49.34 C
ATOM 176 C SER A 22 46.602 -2.653 52.834 1.00 49.48 C
ATOM 177 O SER A 22 47.812 -2.706 53.055 1.00 50.86 O
ATOM 178 CB SER A 22 46.448 -5.048 53.679 1.00 48.97 C
ATOM 179 OG SER A 22 45.640 -6.064 54.237 0.00 50.60 O
ATOM 180 N PRO A 23 46.022 -1.898 52.058 0.00 49.85 N
ATOM 181 CA PRO A 23 46.872 -0.901 51.412 0.00 49.58 C
ATOM 182 C PRO A 23 47.830 -0.288 52.469 0.00 48.84 C
ATOM 183 O PRO A 23 47.512 -0.405 53.659 0.00 48.83 O
ATOM 184 CB PRO A 23 45.846 0.084 50.804 0.00 49.34 C
ATOM 185 CG PRO A 23 44.633 -0.111 51.615 0.00 50.09 C
ATOM 186 CD PRO A 23 44.592 -1.576 51.919 0.00 50.42 C
ATOM 187 N LEU A 24 49.041 0.199 52.104 1.00 44.44 N
ATOM 188 CA LEU A 24 50.042 0.871 52.961 1.00 44.58 C
ATOM 189 C LEU A 24 50.280 2.299 52.591 1.00 43.39 C
ATOM 190 O LEU A 24 50.340 2.606 51.396 1.00 43.10 O
ATOM 191 CB LEU A 24 51.304 0.038 53.127 1.00 45.04 C
ATOM 192 CG LEU A 24 51.343 -1.457 53.404 1.00 46.38 C
ATOM 193 CD1 LEU A 24 52.778 -1.917 53.205 1.00 48.29 C
ATOM 194 CD2 LEU A 24 50.873 -1.770 54.797 1.00 46.87 C
ATOM 195 N PRO A 25 50.649 3.088 53.576 1.00 41.73 N